The conditions required for the formation of precipitin between guinea-pig collagen and rabbit antibodies were investigated. The amount of precipitin was found to be inversely related to the ionic strength of the solution and, to a lesser extent, inversely related to temperature. Gelatin, the heat-denatured form of collagen, could also form precipitins with anti-collagen, suggesting that the quaternary and tertiary structures of collagen played little or no role in the recognition and binding with the anti-collagen sera used. © 1968.